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Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']

 SPIKE_MERS1             Reviewed;        1353 AA.
K9N5Q8;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
06-MAR-2013, sequence version 1.
07-APR-2021, entry version 53.
RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04099};
AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04099};
Contains:
RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04099};
Contains:
RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04099};
Contains:
RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04099};
Flags: Precursor;
Name=S {ECO:0000255|HAMAP-Rule:MF_04099}; ORFNames=3;
Middle East respiratory syndrome-related coronavirus (isolate United
Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1).
Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
Betacoronavirus; Merbecovirus.
NCBI_TaxID=1263720;
NCBI_TaxID=9838; Camelus dromedarius (Dromedary) (Arabian camel).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=23078800;
Bermingham A., Chand M.A., Brown C.S., Aarons E., Tong C., Langrish C.,
Hoschler K., Brown K., Galiano M., Myers R., Pebody R.G., Green H.K.,
Boddington N.L., Gopal R., Price N., Newsholme W., Drosten C.,
Fouchier R.A., Zambon M.;
"Severe respiratory illness caused by a novel coronavirus, in a patient
transferred to the United Kingdom from the Middle East, September 2012.";
Eurosurveillance 17:20290-20290(2012).
[2]
FUNCTION, AND INTERACTION WITH HOST DPP4.
PubMed=23486063; DOI=10.1038/nature12005;
Raj V.S., Mou H., Smits S.L., Dekkers D.H., Muller M.A., Dijkman R.,
Muth D., Demmers J.A., Zaki A., Fouchier R.A., Thiel V., Drosten C.,
Rottier P.J., Osterhaus A.D., Bosch B.J., Haagmans B.L.;
"Dipeptidyl peptidase 4 is a functional receptor for the emerging human
coronavirus-EMC.";
Nature 495:251-254(2013).
-!- FUNCTION: [Spike protein S1]: attaches the virion to the cell membrane
by interacting with host receptor, initiating the infection (By
similarity). Interacts with host DPP4 to mediate virla entry.
{ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:23486063}.
-!- FUNCTION: [Spike protein S2]: mediates fusion of the virion and
cellular membranes by acting as a class I viral fusion protein. Under
the current model, the protein has at least three conformational
states: pre-fusion native state, pre-hairpin intermediate state, and
post-fusion hairpin state. During viral and target cell membrane
fusion, the coiled coil regions (heptad repeats) assume a trimer-of-
hairpins structure, positioning the fusion peptide in close proximity
to the C-terminal region of the ectodomain. The formation of this
structure appears to drive apposition and subsequent fusion of viral
and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}.
-!- FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is
unmasked following S2 cleavage occurring upon virus endocytosis.
{ECO:0000255|HAMAP-Rule:MF_04099}.
-!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit.
The resulting peplomers protrude from the virus surface as spikes. S1
interacts with murine DPP4. {ECO:0000255|HAMAP-Rule:MF_04099,
ECO:0000269|PubMed:23486063}.
-!- INTERACTION:
K9N5Q8; M1PFC6: DPP4; Xeno; NbExp=2; IntAct=EBI-25474996, EBI-25570499;
K9N5Q8; P27487: DPP4; Xeno; NbExp=7; IntAct=EBI-25474996, EBI-2871277;
K9N5Q8; P09958: FURIN; Xeno; NbExp=3; IntAct=EBI-25474996, EBI-1056807;
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate
compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass
type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell
membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the
endoplasmic reticulum-Golgi intermediate compartment, where it
participates in virus particle assembly. Some S oligomers are
transported to the host plasma membrane, where they may mediate cell-
cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099}.
-!- DOMAIN: Fusion peptide 1 (FP1) and fusion peptide 2 (FP2) function
cooperatively and have a membrane-ordering effect on lipid headgroups
and shallow hydrophobic regions of target bilayers. They are considered
as two domains of an extended, bipartite FP. The membrane-ordering
activity is calcium-dependent and also dependent on correct folding,
which is maintained by an internal disulfide bond in FP2.
{ECO:0000255|HAMAP-Rule:MF_04099}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
precursor is processed into S1 and S2 by host cell furin or another
cellular protease to yield the mature S1 and S2 proteins. Additionally,
a second cleavage leads to the release of a fusion peptide after viral
attachment to host cell receptor. {ECO:0000255|HAMAP-Rule:MF_04099}.
-!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike
glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-
Rule:MF_04099}.
-!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
{ECO:0000255|HAMAP-Rule:MF_04099}.
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EMBL; KC164505; AFY13307.1; -; Genomic_RNA.
PDB; 4L72; X-ray; 3.00 A; B=382-585.
PDB; 4MOD; X-ray; 1.90 A; A/B=992-1055, A/B=1250-1286.
PDB; 4XAK; X-ray; 2.45 A; A/B=367-601.
PDB; 4ZPT; X-ray; 2.59 A; R/S=381-588.
PDB; 4ZPV; X-ray; 3.20 A; R/S=381-588.
PDB; 4ZPW; X-ray; 3.02 A; R/S=381-588.
PDB; 5GMQ; X-ray; 2.70 A; A=366-588.
PDB; 5GR7; X-ray; 2.40 A; C=292-300.
PDB; 5GSB; X-ray; 1.80 A; C=291-300.
PDB; 5GSR; X-ray; 2.20 A; P/Q=292-300.
PDB; 5GSV; X-ray; 2.00 A; C=1191-1200.
PDB; 5GSX; X-ray; 2.50 A; C/F=1191-1200.
PDB; 5VYH; X-ray; 2.00 A; A=18-353.
PDB; 5W9H; EM; 4.00 A; A/D/G/p/q/r=1-1291.
PDB; 5W9I; EM; 3.60 A; A/B/E/F/I/J=1-1291.
PDB; 5W9J; EM; 4.80 A; A/D/G/J/K/L=1-1291.
PDB; 5W9K; EM; 4.60 A; A/D/G/J/K/L=1-1291.
PDB; 5W9L; EM; 4.80 A; A/B/C/D/G/J=1-1291.
PDB; 5W9M; EM; 4.70 A; A/D/E/F/G/J=1-1291.
PDB; 5W9N; EM; 5.00 A; A/D/G/H/I/J=1-1291.
PDB; 5W9O; EM; 4.50 A; A/D/G/J/K/L=1-1291.
PDB; 5W9P; EM; 4.00 A; A/B/C/H/I/J=1-1291.
PDB; 5X4R; X-ray; 1.50 A; A=18-353.
PDB; 5X59; EM; 3.70 A; A/B/C=18-1294.
PDB; 5X5C; EM; 4.10 A; A/B/C=18-1294.
PDB; 5X5F; EM; 4.20 A; A/B/C=18-1294.
PDB; 5YY5; X-ray; 2.80 A; A/B=380-588.
PDB; 5ZVK; X-ray; 3.31 A; A/B/C=984-1062.
PDB; 5ZXV; X-ray; 4.48 A; A/B=381-588.
PDB; 6C6Y; X-ray; 3.32 A; R/S=381-588.
PDB; 6C6Z; X-ray; 2.10 A; A/B=367-589.
PDB; 6J11; X-ray; 3.00 A; A/B/C=18-353.
PDB; 6J2J; X-ray; 2.50 A; C/F=422-430.
PDB; 6L8Q; X-ray; 3.10 A; B/D/F/H=367-606.
PDB; 6PXH; X-ray; 2.30 A; A/B=18-351.
PDB; 6WAR; X-ray; 3.40 A; A/C/E/G/I/K/M/O=367-589.
PDBsum; 4L72; -.
PDBsum; 4MOD; -.
PDBsum; 4XAK; -.
PDBsum; 4ZPT; -.
PDBsum; 4ZPV; -.
PDBsum; 4ZPW; -.
PDBsum; 5GMQ; -.
PDBsum; 5GR7; -.
PDBsum; 5GSB; -.
PDBsum; 5GSR; -.
PDBsum; 5GSV; -.
PDBsum; 5GSX; -.
PDBsum; 5VYH; -.
PDBsum; 5W9H; -.
PDBsum; 5W9I; -.
PDBsum; 5W9J; -.
PDBsum; 5W9K; -.
PDBsum; 5W9L; -.
PDBsum; 5W9M; -.
PDBsum; 5W9N; -.
PDBsum; 5W9O; -.
PDBsum; 5W9P; -.
PDBsum; 5X4R; -.
PDBsum; 5X59; -.
PDBsum; 5X5C; -.
PDBsum; 5X5F; -.
PDBsum; 5YY5; -.
PDBsum; 5ZVK; -.
PDBsum; 5ZXV; -.
PDBsum; 6C6Y; -.
PDBsum; 6C6Z; -.
PDBsum; 6J11; -.
PDBsum; 6J2J; -.
PDBsum; 6L8Q; -.
PDBsum; 6PXH; -.
PDBsum; 6WAR; -.
SMR; K9N5Q8; -.
BioGRID; 4383879; 6.
ComplexPortal; CPX-5766; MERS-CoV Spike protein complex.
IntAct; K9N5Q8; 6.
BindingDB; K9N5Q8; -.
ABCD; K9N5Q8; 129 sequenced antibodies.
Proteomes; UP000139997; Genome.
GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-UniRule.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:UniProtKB-UniRule.
CDD; cd21486; human_MERS-CoV_Spike_S1_RBD; 1.
CDD; cd21626; MERS-CoV-like_Spike_S1_NTD; 1.
DisProt; DP02880; -.
Gene3D; 1.20.5.790; -; 1.
HAMAP; MF_04099; BETA_CORONA_SPIKE; 1.
InterPro; IPR032500; bCoV_S1_N.
InterPro; IPR042578; BETA_CORONA_SPIKE.
InterPro; IPR043607; CoV_S1_C.
InterPro; IPR043473; S2_sf_CoV.
InterPro; IPR027400; S_HR2_CoV.
InterPro; IPR036326; Spike_rcpt-bd_sf_CoV.
InterPro; IPR044337; Spike_S1_N_MERS-CoV-like.
InterPro; IPR018548; Spike_S1_RBD_bCoV.
InterPro; IPR044376; Spike_S1_RBD_MERS-CoV.
InterPro; IPR002552; Spike_S2_CoV.
InterPro; IPR043614; Spike_S2_CoV_C.
Pfam; PF16451; bCoV_S1_N; 1.
Pfam; PF09408; bCoV_S1_RBD; 1.
Pfam; PF19209; CoV_S1_C; 1.
Pfam; PF01601; CoV_S2; 1.
Pfam; PF19214; CoV_S2_C; 1.
SUPFAM; SSF111474; SSF111474; 2.
SUPFAM; SSF143587; SSF143587; 1.
PROSITE; PS51921; BCOV_S1_CTD; 1.
PROSITE; PS51922; BCOV_S1_NTD; 1.
PROSITE; PS51923; COV_S2_HR1; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein;
Viral penetration into host cytoplasm; Virion; Virulence;
Virus entry into host cell.
SIGNAL 1..17
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CHAIN 18..1353
/note="Spike glycoprotein"
/id="PRO_0000422465"
CHAIN 18..751
/note="Spike protein S1"
/id="PRO_0000422466"
CHAIN 752..1353
/note="Spike protein S2"
/id="PRO_0000422467"
CHAIN 888..1353
/note="Spike protein S2'"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
/id="PRO_0000444090"
TOPO_DOM 18..1296
/note="Extracellular"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
TRANSMEM 1297..1317
/note="Helical"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
TOPO_DOM 1318..1353
/note="Cytoplasmic"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
DOMAIN 18..351
/note="BetaCoV S1-NTD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
DOMAIN 381..587
/note="BetaCoV S1-CTD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
REGION 367..606
/note="Receptor-binding domain"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
REGION 888..909
/note="Fusion peptide 1"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
REGION 907..929
/note="Fusion peptide 2"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
REGION 994..1044
/note="Heptad repeat 1"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
REGION 1246..1285
/note="Heptad repeat 2"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
COILED 1023..1067
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
COILED 1258..1286
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
MOTIF 1351..1353
/note="KxHxx"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
COMPBIAS 1313..1337
/note="Cys-rich"
SITE 751..752
/note="Cleavage; by host"
/evidence="ECO:0000250"
SITE 887..888
/note="Cleavage"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 66
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 104
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 125
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 155
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 166
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 222
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 236
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 244
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 410
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 487
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 592
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 619
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 719
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 774
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 785
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 870
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 1176
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 1213
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 1225
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 1241
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 1256
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 1277
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
CARBOHYD 1288
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
DISULFID 185..237
/evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
DISULFID 339..349
/evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
DISULFID 383..407
/evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
DISULFID 425..478
/evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
DISULFID 437..585
/evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
DISULFID 912..925
/evidence="ECO:0000255|HAMAP-Rule:MF_04099"
STRAND 27..29
/evidence="ECO:0007744|PDB:6PXH"
STRAND 33..35
/evidence="ECO:0007744|PDB:5X4R"
HELIX 37..40
/evidence="ECO:0007744|PDB:5X4R"
HELIX 50..52
/evidence="ECO:0007744|PDB:5X4R"
TURN 53..55
/evidence="ECO:0007744|PDB:5X4R"
STRAND 66..75
/evidence="ECO:0007744|PDB:5X4R"
STRAND 83..85
/evidence="ECO:0007744|PDB:5X4R"
STRAND 92..95
/evidence="ECO:0007744|PDB:6J11"
STRAND 99..102
/evidence="ECO:0007744|PDB:5X4R"
HELIX 105..107
/evidence="ECO:0007744|PDB:5X4R"
STRAND 116..121
/evidence="ECO:0007744|PDB:5X4R"
TURN 122..125
/evidence="ECO:0007744|PDB:5X4R"
STRAND 126..129
/evidence="ECO:0007744|PDB:5X4R"
STRAND 131..133
/evidence="ECO:0007744|PDB:5X4R"
STRAND 137..141
/evidence="ECO:0007744|PDB:5X4R"
STRAND 147..151
/evidence="ECO:0007744|PDB:5X4R"
STRAND 153..155
/evidence="ECO:0007744|PDB:5X4R"
STRAND 161..164
/evidence="ECO:0007744|PDB:5X4R"
STRAND 166..174
/evidence="ECO:0007744|PDB:5X4R"
TURN 175..178
/evidence="ECO:0007744|PDB:5X4R"
STRAND 179..189
/evidence="ECO:0007744|PDB:5X4R"
STRAND 198..200
/evidence="ECO:0007744|PDB:6PXH"
STRAND 206..208
/evidence="ECO:0007744|PDB:5X4R"
HELIX 210..213
/evidence="ECO:0007744|PDB:5X4R"
HELIX 223..231
/evidence="ECO:0007744|PDB:5X4R"
STRAND 232..244
/evidence="ECO:0007744|PDB:5X4R"
STRAND 252..259
/evidence="ECO:0007744|PDB:5X4R"
STRAND 262..268
/evidence="ECO:0007744|PDB:5X4R"
TURN 269..271
/evidence="ECO:0007744|PDB:5X4R"
TURN 273..275
/evidence="ECO:0007744|PDB:5X4R"
STRAND 278..284
/evidence="ECO:0007744|PDB:5X4R"
STRAND 292..295
/evidence="ECO:0007744|PDB:5X4R"
STRAND 298..300
/evidence="ECO:0007744|PDB:5X4R"
HELIX 304..306
/evidence="ECO:0007744|PDB:5X4R"
STRAND 313..317
/evidence="ECO:0007744|PDB:5X4R"
STRAND 319..327
/evidence="ECO:0007744|PDB:5X4R"
STRAND 333..338
/evidence="ECO:0007744|PDB:5X4R"
HELIX 339..341
/evidence="ECO:0007744|PDB:5X4R"
HELIX 343..349
/evidence="ECO:0007744|PDB:5X4R"
TURN 351..353
/evidence="ECO:0007744|PDB:5VYH"
HELIX 386..389
/evidence="ECO:0007744|PDB:6C6Z"
HELIX 396..398
/evidence="ECO:0007744|PDB:6C6Z"
STRAND 400..404
/evidence="ECO:0007744|PDB:6C6Z"
STRAND 406..408
/evidence="ECO:0007744|PDB:6C6Z"
HELIX 411..415
/evidence="ECO:0007744|PDB:6C6Z"
STRAND 418..426
/evidence="ECO:0007744|PDB:6C6Z"
TURN 430..434
/evidence="ECO:0007744|PDB:4XAK"
STRAND 440..447
/evidence="ECO:0007744|PDB:6C6Z"
HELIX 450..455
/evidence="ECO:0007744|PDB:6C6Z"
STRAND 456..459
/evidence="ECO:0007744|PDB:6C6Z"
HELIX 463..467
/evidence="ECO:0007744|PDB:6C6Z"
STRAND 473..475
/evidence="ECO:0007744|PDB:6C6Z"
STRAND 477..483
/evidence="ECO:0007744|PDB:6C6Z"
STRAND 495..506
/evidence="ECO:0007744|PDB:6C6Z"
STRAND 508..510
/evidence="ECO:0007744|PDB:4ZPV"
STRAND 513..515
/evidence="ECO:0007744|PDB:6C6Z"
HELIX 525..528
/evidence="ECO:0007744|PDB:6C6Z"
STRAND 540..544
/evidence="ECO:0007744|PDB:6C6Z"
TURN 547..550
/evidence="ECO:0007744|PDB:6C6Z"
STRAND 551..562
/evidence="ECO:0007744|PDB:6C6Z"
STRAND 568..576
/evidence="ECO:0007744|PDB:6C6Z"
STRAND 584..586
/evidence="ECO:0007744|PDB:4XAK"
HELIX 995..1038
/evidence="ECO:0007744|PDB:4MOD"
HELIX 1263..1277
/evidence="ECO:0007744|PDB:4MOD"
SEQUENCE 1353 AA; 149411 MW; D73276432FA5D515 CRC64;
MIHSVFLLMF LLTPTESYVD VGPDSVKSAC IEVDIQQTFF DKTWPRPIDV SKADGIIYPQ
GRTYSNITIT YQGLFPYQGD HGDMYVYSAG HATGTTPQKL FVANYSQDVK QFANGFVVRI
GAAANSTGTV IISPSTSATI RKIYPAFMLG SSVGNFSDGK MGRFFNHTLV LLPDGCGTLL
RAFYCILEPR SGNHCPAGNS YTSFATYHTP ATDCSDGNYN RNASLNSFKE YFNLRNCTFM
YTYNITEDEI LEWFGITQTA QGVHLFSSRY VDLYGGNMFQ FATLPVYDTI KYYSIIPHSI
RSIQSDRKAW AAFYVYKLQP LTFLLDFSVD GYIRRAIDCG FNDLSQLHCS YESFDVESGV
YSVSSFEAKP SGSVVEQAEG VECDFSPLLS GTPPQVYNFK RLVFTNCNYN LTKLLSLFSV
NDFTCSQISP AAIASNCYSS LILDYFSYPL SMKSDLSVSS AGPISQFNYK QSFSNPTCLI
LATVPHNLTT ITKPLKYSYI NKCSRFLSDD RTEVPQLVNA NQYSPCVSIV PSTVWEDGDY
YRKQLSPLEG GGWLVASGST VAMTEQLQMG FGITVQYGTD TNSVCPKLEF ANDTKIASQL
GNCVEYSLYG VSGRGVFQNC TAVGVRQQRF VYDAYQNLVG YYSDDGNYYC LRACVSVPVS
VIYDKETKTH ATLFGSVACE HISSTMSQYS RSTRSMLKRR DSTYGPLQTP VGCVLGLVNS
SLFVEDCKLP LGQSLCALPD TPSTLTPRSV RSVPGEMRLA SIAFNHPIQV DQLNSSYFKL
SIPTNFSFGV TQEYIQTTIQ KVTVDCKQYV CNGFQKCEQL LREYGQFCSK INQALHGANL
RQDDSVRNLF ASVKSSQSSP IIPGFGGDFN LTLLEPVSIS TGSRSARSAI EDLLFDKVTI
ADPGYMQGYD DCMQQGPASA RDLICAQYVA GYKVLPPLMD VNMEAAYTSS LLGSIAGVGW
TAGLSSFAAI PFAQSIFYRL NGVGITQQVL SENQKLIANK FNQALGAMQT GFTTTNEAFH
KVQDAVNNNA QALSKLASEL SNTFGAISAS IGDIIQRLDV LEQDAQIDRL INGRLTTLNA
FVAQQLVRSE SAALSAQLAK DKVNECVKAQ SKRSGFCGQG THIVSFVVNA PNGLYFMHVG
YYPSNHIEVV SAYGLCDAAN PTNCIAPVNG YFIKTNNTRI VDEWSYTGSS FYAPEPITSL
NTKYVAPQVT YQNISTNLPP PLLGNSTGID FQDELDEFFK NVSTSIPNFG SLTQINTTLL
DLTYEMLSLQ QVVKALNESY IDLKELGNYT YYNKWPWYIW LGFIAGLVAL ALCVFFILCC
TGCGTNCMGK LKCNRCCDRY EEYDLEPHKV HVH


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